Crystal Structure of the Complex Formed Between Bovine β-Trypsin and MCTI-A, a Trypsin Inhibitor of Squash Family, at 1.8-Å Resolution

The stoichiometric complex formed between bovine β-trypsin and Momordica charantia, Linn. Cucurbitaceae trypsin inhibitor A (MCTI-A) was crystallized and its X-ray crystal structure was refined to a final R value of 0.179 using data of 7.0- to 1.8-Å resolution. Combination with results on the complex of MCTI-A with porcine trypsin gives the sequence of MCTI-A definitely, of which 13 residues are conserved compared with other squash family trypsin inhibitors. Its spatial structure and the conformation of its primary binding segment from Cys3I (P3) to Glu7I (P3′), which contains a reactive scissile bond Arg5I C–Ile6I N, were found to be very similar to the other squash family proteinase inhibitors.